Structural investigations of the RBD‐ACE2 complex provided information about essential residues for viral entry. Hsiang et al. 35  reported a number of peptides that significantly blocked the interaction of the S protein with ACE2 with IC50 values as low as 1.88 nM. Michael et al. found charged residues between positions 22 and 57 crucial for SARS‐CoV‐1 viral entry. Based on this, they designed peptides P4 (IC50, 50 µM) and P5 (IC50, 6.0 µM) with significant inhibitory activity against SARS‐CoV‐1. The antiviral activity was further improved when they introduced the glycine binding linkage of peptide P4 (residues 22–47) with an ACE2‐derived peptide (residues 351–357) against a SARS‐CoV‐1 pseudovirus with an IC50 of 100 nM and devoid of cytotoxicity up to 200 µM. 36  It is worth highlighting that a similar strategy could work for the new SARS‐CoV‐2. The recently solved cryo‐EM structure of SARS‐CoV‐2 in complex with human ACE2 can provide a structural rationale for the peptide design. 29